• Journal of Microbiology and Biotechnology
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• v.33 no.10
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• pp.1390-1401
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• 2023

In this study, a 12-week feeding experiment was conducted to characterize the effects of exogenous α-amylase on the growth, feed utilization, digestibility, plasma α-amylase activity, feed degradation rate, and fecal particle size of olive flounder (Paralichthys olivaceus). Diet was supplemented with 0 (AA₀; control), 100 (AA₁₀₀), 200 (AA₂₀₀), or 400 (AA₄₀₀) mg/kg of α-amylase, respectively. Fish (273.1 ± 2.3 g) were stocked into 12 tanks (25 fish/1,000-L tank) and 3 tanks were randomly selected for each diet group. As a result, α-amylase was found to have no significant effects (p ≥ 0.05) on the growth, feed utilization parameters, and whole-body proximate compositions. α-Amylase-treated fish exhibited only a significant increase in the apparent digestibility coefficient of carbohydrates compared to the controls. In addition, in vitro analyses revealed that α-amylase dose-dependently increased (p < 0.05) the feed degradation rate, while photographs of the intestinal content after 2, 4, and 8 h of feeding demonstrated an improved degradation rate in the α-amylase-treated groups. Plasma α-amylase content was higher in the AA₂₀₀ and AA₄₀₀ groups, whereas the control group produced significantly larger-sized fecal particles (90% size class) than these two groups. In the intestine, no changes were observed in the expression levels of the immune-related TNF-α, IL-1β, IL-2, immunoglobulin-M, HSP-70, lysozyme, and amylase alpha-2A. However, growth-related genes IGF-1, IGF-2, TGF-β3, and growth hormone genes were upregulated in muscle tissues. Collectively, exogenous α-amylase has positive roles in the modulation of the digestibility coefficient, blood α-amylase concentration, growth-related gene expression, and diet degradation for improved digestion in olive flounder.

• Microbiology and Biotechnology Letters
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• v.10 no.4
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• pp.259-265
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• 1982

These experiments were conducted to investigate the hydrolysis products on the various oligosaccharides of Bacillus cirulans F-2 $\alpha$-amylase, and the hydrolysis rate on the various raw starches of Bacillus circulans F-2 $\alpha$-amylase, Bacillus amylotiquefaciens $\alpha$-amylase and Rhizopus niveus glucoamylase. The results obtained were as follows : 1. Maltotetraose, maltopentaose, maltohexaose, maltoheptaose and maltooctaose were hydrolyzed, but maltose and maltotriose were not hydrolyzed by Bacillus circulans F-2 $\alpha$-amylase. Among maltotetraose, maltopentaose, maltohexaose, maltoheptaose and maltooctaose, especially maltotetraose was hydrolyzed weakly by Bacillus circulans F-2 $\alpha$-amylase. 2. The Hydrolysis rate of oyster glycogen was slightly lower than soluble starch, amylose and amylopectin. 3. The hydrolysis rate of com starch was higher in shaking incubation than in stationary incubation, but the hydrolysis rate of potato starch was not definite according to kinds of enzyme. 4. On com, rice, arrowroot, high amylose corn, banana, sago, yam and potato starch, Bacillus circulans F-2 $\alpha$-amylase exhibited a remarkably higher hydrolysis rate than Bacillus amyloquefaciems $\alpha$-amylase and Rhizopus niveus glucoamylase.

• Microbiology and Biotechnology Letters
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• v.13 no.3
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• pp.223-232
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• 1985

To find microorganisms of producing $\alpha$-amylase inhibitors, actinomycetes were isolated from soil samples that were collected at different locations in Korea and screened for enzyme inhibitory activity. A strain of these microbes had a high inhibitory activity and was identified as one of the genus Streptomyces by morphological, biochemical and physiological studies according to the methods of the International Streptomyces Project (ISP). The medium used consisted of 3 ％ corn starch, 0.2％ yeast extract and 0.8％ peptone (pH 7.0). When this strain was aerobically cultured in the medium on a rotary shaker, the highest inhibitory activity was obtained after four days. This inhibitor had inhibitory activities on various $\alpha$-amylases and glucoamylase, but not on $\beta$-amylase.

• KSBB Journal
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• v.19 no.4
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• pp.301-307
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• 2004

The characteristics of the a-amylase of Aspergillus coreanus NR 15-1 isolated from traditional Korean Nuruk have been carried out. The a-amylase of A. coreanus NR 15-1 was purified by ammonium sulfate precipitation followed by column chromatographies on CM-cellulose, DEAE-cellulose, Sephadex G-100 gel filtration and hydroxyapatite. The a-amylase was purified 78-fold with a yield of 8.7%. The molecular weight of the a-amylase was estimated to be 49 kDa by Sephadex G-100 gel filtration and 51 kDa by SDS-polyacrylamide gel eletrophoresis. These experimental results suggested that the purified enzyme might be monomer. The enzyme was stable between pH 4 and 11. The optimum pH was 5.0. The optimum temperature for enzyme was 45$^{\circ}C$ and the enzyme was stable up to 50$^{\circ}C$. The enzyme was significantly inhibited by 1 mM N-bromosuccinimide. These results suggested that tryptophan residue was involved in the active site of a-amylase. The enzyme was identified as a-amylase because the reaction products of soluble starch hydrolyzed by the purified enzyme was oligosaccharide by thin layer chromatography.

• KSBB Journal
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• v.18 no.5
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• pp.363-370
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• 2003

A filamentous fungus, strain FM04 producing amylase was isolated from rotten yam peels and potatoes. The favorable conditions of cultivation factors such as, temperature, pH, and agitation speed of strain FM04 were 28∼30$^{\circ}C$, 5.0∼6.0, and 100 rpm, respectively. Starch was the best carbon source in the amylase production. Therefore, food wastes containing lots of starch were employed as the carbon source of the cultivation for the economical amylase production. 5.2 U/ml of amylase was obtained In the cultivation using 1 % (w/v) of food wastes. The amylase showed the highest activity at enzyme reaction conditions of 60$^{\circ}C$ and pH 4.5 and showed 90% of residual activity after the reaction at 50$^{\circ}C$ for 2 days. In the enzymatic hydrolysis reaction using 20% (w/v) of food wastes and 2.5 U/ml of amylase, 72.6 g/l of reducing sugar was obtained at the reaction condition of 50$^{\circ}C$, pH 4.5 for 2 days.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.8
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• pp.1262-1269
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• 2003

In this study, enzymes were investigated as an antistaling agent for a Korean rice cake. Thermograms by a DSC demonstrated that the gelatinization-onset temperature of the Korean rice cake was at its lowest temperature of 71.1$^{\circ}C$ with the GP (glucoamylase+pullulanase) treatment, followed by $\beta$-amylase and $\alpha$-amylase. The gelatinization peak temperature of the Korean rice cake with enzyme treatment was relatively lower compared to the control. Furthermore, the Korean rice cake with GP treatment showed the lowest peak temperature. Melting enthalpy of the Korean rice cake increased with the enzyme treatment, with $\beta$-amylase, followed by $\alpha$-amylase and GP. Melting enthalpy of the Korean rice cake with GP treatment was significantly lower compared to the $\beta$- and $\alpha$-amylase treatment. Recrystallinity in the case of GP treatment was also significantly lower than control. The range of Avrami exponent (n) was 0.90 ∼ 1.20 and the time constant of retrogradation (1/k) of the Korean rice cake crystalline decreased in the following order: GP, $\beta$-, $\alpha$ -amylase and control. Textural characteristics of the Korean rice cake with enzyme treatment differed greatly from that of control. The L＊ values of all the Korean rice cakes made without $\beta$-amylase decreased and the a＊ values were significantly different at p<0.05. The GP treatment altered the b＊ value toward blue color, whereas $\beta$-and $\alpha$-amylase changed to the direction to yellow color. In sensory evaluation, the Korean rice cake with enzyme treatment showed higher evaluation compared to control.

• Journal of Chest Surgery
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• v.28 no.10
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• pp.892-899
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• 1995

Pancreatitis is a known complication of cardiac surgery with cardiopulmonary bypass. Although ischemia is believed to be a factor, the exact cause of pancreatitis after cardiopulmonary bypass remains unknown.We prospectively studied 67 consecutive patients undergoing cardiac surgery with cardiopulmonary bypass for evaluation of the pancreatic injury after cardiopulmonary bypas. Serial measurement of amylase level in serum and urine was done postoperatively. Hyperamylasemia was detected in 15 patients[22.4% , of whom no patient had pancreatitis. There was no significant difference between serum amylase level and parameters such as cardiopulmonay bypass time, aortic cross clamp time, mean blood pressure, rectal temperature, flow rate, and use of circulatory arrest during cardiopulmonary bypass. Hyperamylasuria was detected in 8 patients[11.9% , and urine amylase level was elevated significantly in the groups with prolonged cardiopulmonary bypass, mean blood pressure more than 40mmHg, and rectal temperature more than 20 $^{\circ}$C. We recommend that serum amylase level and/or amylase-creatinine clearance ratio is measured for ealy detection and management of pancreatitis after cardiopulmonary bypass.

• Archives of Pharmacal Research
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• v.8 no.2
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• pp.67-75
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• 1985

To find emylase inhibitors produced by microorganisms from soil, a strain which had a strong inhibitory activity against bacteria .alpha.-amylase was isolated from the soil smaple collected in Seoul. The morphological and physiological characteristics of this strain on several media and its utilization of carbon sources showed that it was one of Streptomyces specties according to the international Streptomyces Project method. The amylase inhibitor of this strain was purified by means of acetone precipitation, adsorption on Amberlite XAD-2, and column chromatography on Amberlite CG-50 and SP-Sephadex C-25. The inhibitor was stable at the pH range of 1-10 and at 100.deg.C for half an hour, and had inhibitory activities against other amylases such as salivary .alpha.-amylase, pancreatic .alpha.-amylase, fungal .alpha.-amylase and glucoamylase. The kinetic studies of the inhibitor showed that its inhibitory effect on starch hydrolysis by .alpha.-amylase was non-competitive.

• Microbiology and Biotechnology Letters
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• v.14 no.2
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• pp.155-160
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• 1986

$\alpha$-Amylase gene of B. amyloliquefaciens was cloned to E. coli-yeast shuttle vector YEp-13 and expressed in E. coli. Chromosomal DNA of B. amyloliquefaciens was partially digested with Sau3Al and YEp13 plasmid was cleaved with BamH1. The hybrid plasmid, pHA28, was constructed by shotgun method and transformed to E. coli C600 and HB101. The amount of $\alpha$-amylase produced by transformants of E. coli was about 20% to 30% of that produced by B. amyloli-quefaciens. About 65% of $\alpha$-amylase produced by transformant was secreted into periplasm and the others were located in cytoplasm. $\alpha$-Amylase production was maximal when transformants were cultivated for 15hr to 20hr. As the result of agarose gel electrophoresis, pHA28 plasmid was found to be various in its size. This result suggested that pHA28 plasmid was segregated.

• Microbiology and Biotechnology Letters
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• v.19 no.5
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• pp.464-469
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• 1991

An $\alpha$-amylase producing bacterium, strain 2B, was isolated from soil and identified to genus Bacillus. To enhance $\alpha$-amylase productivity, strain 2B was mutagenized successively with nitrosoguanidine. For an efficient selection of a-amylase hyperproducers, mutants which produced $\alpha$-amylase in the presence of glucose were isolated. The resultant mutant HG4, which was classified as constitutive and catabolite derepressed hyperproducer of a-amylase, produced about 30 folds more $\alpha$-amylase than parental strain in medium containing lactose as carbon source. The strain HG4 grew rapidly and produced enzyme in parallel with cell growth. Moreover, its cell lysis did not occur until time of maximal yield of enzyme, which was considered to be a favorable characteristic for the production and purificiation of enzyme in industrial scale. The enzymatic properties of parental strain 2B and mutant strain HG4 were almost the same. The optimal temperature and pH for enzyme reaction was $70^{\circ}C$ and pH 6.0, respectively, in 'the presence of 0.6mM $Ca^[2+}$ as an effective stabilizer.